ID   ATP6_RICPR              Reviewed;         242 AA.
AC   Q9ZEC1;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   27-MAR-2024, entry version 124.
DE   RecName: Full=ATP synthase subunit a {ECO:0000255|HAMAP-Rule:MF_01393};
DE   AltName: Full=ATP synthase F0 sector subunit a {ECO:0000255|HAMAP-Rule:MF_01393};
DE   AltName: Full=F-ATPase subunit 6 {ECO:0000255|HAMAP-Rule:MF_01393};
GN   Name=atpB {ECO:0000255|HAMAP-Rule:MF_01393}; OrderedLocusNames=RP023;
OS   Rickettsia prowazekii (strain Madrid E).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX   NCBI_TaxID=272947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Madrid E;
RX   PubMed=9823893; DOI=10.1038/24094;
RA   Andersson S.G.E., Zomorodipour A., Andersson J.O., Sicheritz-Ponten T.,
RA   Alsmark U.C.M., Podowski R.M., Naeslund A.K., Eriksson A.-S., Winkler H.H.,
RA   Kurland C.G.;
RT   "The genome sequence of Rickettsia prowazekii and the origin of
RT   mitochondria.";
RL   Nature 396:133-140(1998).
CC   -!- FUNCTION: Key component of the proton channel; it plays a direct role
CC       in the translocation of protons across the membrane.
CC       {ECO:0000255|HAMAP-Rule:MF_01393}.
CC   -!- SUBUNIT: F-type ATPases have 2 components, CF(1) - the catalytic core
CC       - and CF(0) - the membrane proton channel. CF(1) has five subunits:
CC       alpha(3), beta(3), gamma(1), delta(1), epsilon(1). CF(0) has three main
CC       subunits: a(1), b(2) and c(9-12). The alpha and beta chains form an
CC       alternating ring which encloses part of the gamma chain. CF(1) is
CC       attached to CF(0) by a central stalk formed by the gamma and epsilon
CC       chains, while a peripheral stalk is formed by the delta and b chains.
CC       {ECO:0000255|HAMAP-Rule:MF_01393}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01393}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01393}.
CC   -!- SIMILARITY: Belongs to the ATPase A chain family. {ECO:0000255|HAMAP-
CC       Rule:MF_01393}.
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DR   EMBL; AJ235270; CAA14494.1; -; Genomic_DNA.
DR   PIR; G71709; G71709.
DR   RefSeq; NP_220417.1; NC_000963.1.
DR   RefSeq; WP_004596667.1; NC_000963.1.
DR   AlphaFoldDB; Q9ZEC1; -.
DR   SMR; Q9ZEC1; -.
DR   STRING; 272947.gene:17555106; -.
DR   EnsemblBacteria; CAA14494; CAA14494; CAA14494.
DR   GeneID; 57569152; -.
DR   KEGG; rpr:RP023; -.
DR   PATRIC; fig|272947.5.peg.23; -.
DR   eggNOG; COG0356; Bacteria.
DR   HOGENOM; CLU_041018_0_2_5; -.
DR   OrthoDB; 9809130at2; -.
DR   Proteomes; UP000002480; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IEA:UniProtKB-KW.
DR   GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-UniRule.
DR   CDD; cd00310; ATP-synt_Fo_a_6; 1.
DR   Gene3D; 1.20.120.220; ATP synthase, F0 complex, subunit A; 1.
DR   HAMAP; MF_01393; ATP_synth_a_bact; 1.
DR   InterPro; IPR000568; ATP_synth_F0_asu.
DR   InterPro; IPR023011; ATP_synth_F0_asu_AS.
DR   InterPro; IPR045083; ATP_synth_F0_asu_bact/mt.
DR   InterPro; IPR035908; F0_ATP_A_sf.
DR   NCBIfam; TIGR01131; ATP_synt_6_or_A; 1.
DR   PANTHER; PTHR11410; ATP SYNTHASE SUBUNIT A; 1.
DR   PANTHER; PTHR11410:SF0; ATP SYNTHASE SUBUNIT A; 1.
DR   Pfam; PF00119; ATP-synt_A; 1.
DR   PRINTS; PR00123; ATPASEA.
DR   SUPFAM; SSF81336; F1F0 ATP synthase subunit A; 1.
DR   PROSITE; PS00449; ATPASE_A; 1.
PE   3: Inferred from homology;
KW   ATP synthesis; Cell inner membrane; Cell membrane; CF(0);
KW   Hydrogen ion transport; Ion transport; Membrane; Reference proteome;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..242
FT                   /note="ATP synthase subunit a"
FT                   /id="PRO_0000082069"
FT   TRANSMEM        29..49
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT   TRANSMEM        84..104
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT   TRANSMEM        114..134
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT   TRANSMEM        140..160
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT   TRANSMEM        189..209
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
FT   TRANSMEM        210..230
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01393"
SQ   SEQUENCE   242 AA;  27378 MW;  488EE81DE6088613 CRC64;
     MTHSPLIQFN IKKLIDIKMF GFDVSFTNSS IYMLLATTLS LTYLYLAFYN RKLIPSRLQV
     SAEIVYNLVA DMLNQNIGIK GRKFIPLVFS LFIFILFCNL LGMTPYSFTA TSHIIVTFTL
     ALLIFLTVTI VGFIKHGVSF LTLFLPHGTP VWLAPLMIVI ELFTYLARPV SLSLRLAANM
     MAGHVLLKVI ASFTVSLMIY LKFLPIPLMV ILIGFEIFIA ILQAYIFTIL SCMYLNDAIN
     LH
//